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Purine nucleoside hydrolase
Analyse Purine nucleoside hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MAS
- Type
- protein
- Length
- 603 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inosine-uridine nucleoside N-ribohydrolase
- EC
- 3.2.2.1
- UniProt
- Q27546
- Ligands
- K
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inosine-uridine nucleoside N-ribohydrolase (EC 3.2.2.1) | protein | 308 | 39% helix, 17% strand | Q27546 |
| B | Inosine-uridine nucleoside N-ribohydrolase (EC 3.2.2.1) | protein | 295 | 42% helix, 17% strand | Q27546 |
Ligands and binding sites
- K · Potassium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 732 | 0.73 | 0.79 | 84 | empty |
| 2 | 503 | 0.69 | 0.79 | 46 | K |
Interfaces
1 interface between chains.
- A–B · 908 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q27546
- Elsewhere: RCSB PDB 1MAS · PDBe 1MAS · UniProt Q27546
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